@text PLASMEPSIN II FROM PLASMODIUM FALCIPARUM CALLIE BOUNDS *{Kinemage 1}* Plasmepsin II is an aspartic protease that is involved in the degradation of Hemoglobin, which takes place in the acidic digestive vacuole of the parasite. It is made up of 329 amino acids and exists as a monomer. Plasmepsin II has a bilobal shape and a pseudo 2-fold rotation axis. Plasmespin II (view 3) contains two disulfide bridges, one between Cys47-Cys52 and the other between Cys249-Cys285. The bridge between Cys249 and Cys285 is seen in all eukaryotic proteases while the bridge between Cys47 and Cys52 is seen only in mammalian enzymes, suggesting a close evolutionary relationship between malarial enzymes and those found in mammals. The active site (view 4) is made up of Asp 34 and Asp 214, and the initial cleavage of hemoglobin takes place between Phe33 and Leu34 in the hinge region of the alpha chain. This first point of cleavage causes the hemoglobin to unravel exposing other sites for proteolytic attack. The enzyme then cleaves between Thr 108 and Leu 109, Leu 136 and Thr 137 in the alpha chain, and Leu 32 and Val 33 in the beta chain of hemoglobin. A unique feature of Plasmepsin II (view 5) is the substitution of Ser for Thr at residue 215 in the Asp-Thr-Gly signature sequence of the enzyme. This substitution has been noticed at the same position in some retroviral aspartic proteases, but its function us unclear. *{Kinemage 2}* Plasmepsin II consists of regularly occurring secondary structure (view 1). Beta pleated sheets and alpha helices occur throughout the protein. The beta sheet (view 2) consists of three stands running in an anti-parallel fashion, beginning with Lys 72 and ending at Asp 107. The alpha helix (view 3) demonstrates right-handedness and consists of the following residues: Lys 144, Leu 143, Glu 142, Val 141, Val 140, and Ile 142. Switching to the backbone structure, the Beta Hairpin Loop (view 4) is part of the active site. Known as the "flap" it lies perpendicular over the active site and interacts with substrates and inhibitors. This interaction is believed to involve orienting and holding the substrate or inhibitor in the correct position so as to allow for catalysis to take place. Plasmepsin II demonstrates a high sequence homology with mammalian aspartic proteases, seen particularly in the "proline rich" loop (view 5). This structure is homologous with rennin and Cat D structures, which consist of three consecutive proline residues. The proline loop found in Plasmepsin II consists of two proline residues, 297 and 295. Both residues participate in a trans peptide linkage and are separated by Val 296. *{Kinemage 3}* Pepstatin A is a pentapeptide inhibitor of Plasmepsin II. Pepstain A binds in the cleft of Plasmepsin II (view 2) inhibiting the degradation of hemoglobin. Pepstatin A resembles the substrate on which Plasmepsin II acts, making it a competitive inhibitor. Of even greater importance is the fact that pepstatin A has the geometry of the catalyzed reaction's transition state. The inhibition constant for pepstatin A is 0.006nM. This high potency suggests that pepstatin A could serve as a lead for the design of selective anti-malarial drugs. The aspartic acid residues, 34, and 214, form a triangular bond with Pepstatin at O11. However, they are unable to break the peptide bond between O11 and N14. Hydrogen bonds (view 4 and View 5) between Tyr 192 and O6, Ser 218 and N20, and Ser 79 and O15 help to hold the inhibitor in place and orient the molecule into the correct position. *{Kinemage 4}* Plasmepsin II shows two conformations (view 1). These two conformational states demonstrate the interdomain flexibility of Plasmepsin II. This flexibility allows for structural rearrangement, which facilitates the binding of the enzyme to the hinge region of Hemoglobin. This flexibility also provides evidence of the enzyme's mobile ability. References: Francis, S.E., Banerjee, R., Goldberg, D.E. (1997) Biosynthesis and Maturation of the Malaria Aspartic Hemoglobinases Plasmepsins I and II. J. Biol. Chem. 272, 14961-14968. Goldberg, D.E., Slater, A.F.G., Beavis, R., Chait, B., Cerami, A., Henderson, G.B. (1991) Hemoglobin Degradation in the Human Malaria Pathogen Plasmodium falciparum: A Catabolic Pathway Initiated by a Specific Aspartic Protease. J. Exp. Med. 173, 961-969. Goldberg, D.E., Slater, A.F.G., Cerami, A., Henderson, G.B. (1990) Hemoglobin Degradation in the Malaria Parasite Plasmodium falciparum: An Ordered Process in a Unique Organelle. Proc. Natl. Acad. Sci. USA. 87, 2931-2935. Le Bonniec, S., Deregnaucourt, C., Redeker, V., Banerjee, R., Grelleir, P., Goldberg, D.E., Schrevel, J. (1999) Plasmepsin II, an Acidic Hemoglobinase from the Plasmodium falciparum Food Vacuole, Is Active at Neutral pH on the Host Erythrocyte Membrane Skeleton. J. Biol. Chem. 274, 14218-14223. Silva, A.M., Lee, A.Y., Gulnik, S.V., Majer, P., Collins, J., Bhat, T.N., Collins, P.J., Cachau, R.E., Luker, K.E., Gluzman, I.Y., Francis, S.E., Oksman, A., Goldberg, D.E., Erickson, J.W. (1996) Structure and Inhibition of Plasmepsin II, a Hemoglobin-Degrading Enzyme from Plasmodium falciparum. Proc. Natl. Acad. Sci. USA. 93, 10034-10039. (Kin 1 coordinates from file: 1QS8.PDB) (Kin 2, 3, 4, coordinates from file 1SME.PDB) @kinemage 1 @caption Plasmepsin II from Plasmodium falciparum Unique components of Plasmepsin II are illustrated including the Disulfide Bonds (yellow), the active aspartic side chains (sea), and the serine substituted side chain (brown). The red balls are the oxygen and hydroxyl groups of each side chain. @onewidth @viewid {Top View} @zoom 1.05 @zslab 225 @ztran 0 @center 53.739 34.618 19.814 @matrix 0.350671 -0.162574 0.922280 -0.929480 -0.180761 0.321545 0.114437 -0.969998 -0.214497 @2viewid {Side View} @2zoom 1.07 @2zslab 200 @2ztran 0 @2center 53.695 40.746 30.813 @2matrix -0.489168 0.823413 0.287586 0.783540 0.559709 -0.269796 -0.383118 0.093359 -0.918969 @3viewid {Disulfide Bond} @3zoom 4.12 @3zslab 200 @3ztran 0 @3center 61.777 56.398 14.045 @3matrix 0.578651 0.770784 -0.266563 -0.701382 0.637094 0.319649 0.416206 0.001996 0.909268 @4viewid {Active Site} @4zoom 5.79 @4zslab 261 @4ztran 0 @4center 57.305 30.868 18.583 @4matrix 0.914281 -0.349017 0.205617 -0.398845 -0.864335 0.306343 0.070802 -0.362093 -0.929450 @5viewid {Ser Substituion} @5zoom 8.20 @5zslab 800 @5ztran 0 @5center 57.412 34.377 22.934 @5matrix 0.571246 0.341929 -0.746166 -0.819998 0.198084 -0.536997 -0.035811 0.918612 0.393536 @master {Calphas} @master {sidechain} @master {hets} @master {atoms} @group {Plasmepsin} @subgroup {mainchain} nobutton @vectorlist {Calphas} color= sky nobutton master= {Calphas} { ca ser a 1 B84.23}P 59.975 28.742 45.262 {"}59.975 28.742 45.262 { ca glu a 2 B74.66}59.272 25.619 43.210 { ca asn a 3 B55.92}58.777 27.672 40.023 { ca asp a 4 B47.46}61.337 26.870 37.363 { ca val a 5 B41.09}62.922 30.059 36.071 { ca ile a 6 B38.16}64.815 30.408 32.787 { ca glu a 7 B39.68}66.645 33.643 32.006 { ca leu a 8 B39.66}66.084 35.299 28.622 { ca asp a 9 B54.08}69.255 36.996 27.371 { ca asp a 10 B61.29}68.972 40.012 25.113 { ca val a 11 B69.65}70.941 40.357 21.872 { ca ala a 12 B71.49}71.160 43.807 20.240 { ca asn a 13 B73.52}67.768 44.500 21.851 { ca ile a 14 B71.53}65.957 42.897 18.908 { ca met a 15 B66.31}65.849 39.244 19.982 { ca phe a 16 B49.76}66.219 37.081 23.092 { ca tyr a 17 B39.90}67.071 33.441 23.696 { ca gly a 18 B35.64}67.297 31.146 26.683 { ca glu a 19 B37.39}69.369 28.142 27.667 { ca gly a 20 B34.34}68.202 24.548 27.485 { ca glu a 21 B41.13}69.866 21.140 27.782 { ca val a 22 B48.43}69.438 17.785 26.047 { ca gly a 23 B49.88}70.932 14.421 26.988 { ca asp a 24 B57.43}72.051 12.973 30.321 { ca asn a 25 B59.46}75.494 14.526 29.748 { ca his a 26 B59.84}73.661 17.867 29.587 { ca gln a 27 B51.97}74.644 19.408 26.243 { ca lys a 28 B47.58}73.762 23.110 26.301 { ca phe a 29 B39.19}71.862 25.045 23.628 { ca met a 30 B39.35}70.629 28.596 23.060 { ca leu a 31 B29.17}66.929 28.282 22.255 { ca ile a 32 B27.07}64.060 30.424 21.070 { ca phe a 33 B28.86}61.178 29.931 23.517 { ca asp a 34 B24.18}58.397 29.992 20.952 { ca thr a 35 B24.06}54.726 30.128 22.031 { ca gly a 36 B17.48}53.953 30.001 18.318 { ca ser a 37 B22.94}55.050 26.385 17.821 { ca ala a 38 B32.47}54.847 23.006 19.585 { ca asn a 39 B30.05}58.016 21.073 18.783 { ca leu a 40 B26.72}61.504 21.126 20.245 { ca trp a 41 B28.11}64.589 20.850 18.059 { ca val a 42 B31.82}68.338 21.369 18.313 { ca pro a 43 B34.53}70.819 21.133 15.437 { ca ser a 44 B40.15}72.201 17.611 15.158 { ca lys a 45 B45.58}75.832 16.496 15.111 { ca lys a 46 B37.49}74.843 14.904 11.793 { ca cys a 47 B43.14}73.857 18.301 10.362 { ca asn a 48 B54.62}75.918 19.287 7.301 { ca ser a 49 B50.12}74.292 22.693 6.846 { ca ser a 50 B42.75}76.822 25.502 6.811 { ca gly a 51 B39.40}74.664 27.192 9.441 { ca cys a 52 B42.31}75.260 24.203 11.689 { ca ser a 53 B46.53}79.027 24.786 11.475 { ca ile a 54 B41.70}78.665 27.718 13.878 { ca lys a 55 B40.72}76.047 26.187 16.169 { ca asn a 56 B41.55}76.109 23.955 19.241 { ca leu a 57 B42.16}75.258 20.496 17.910 { ca tyr a 58 B44.32}73.760 17.468 19.655 { ca asp a 59 B49.66}75.691 14.221 19.834 { ca ser a 60 B49.69}73.296 11.383 20.662 { ca ser a 61 B56.92}76.179 8.966 21.199 { ca lys a 62 B57.52}77.373 10.914 24.243 { ca ser a 63 B57.20}74.090 10.311 26.112 { ca lys a 64 B55.58}73.121 6.997 27.747 { ca ser a 65 B52.54}69.513 8.189 28.041 { ca tyr a 66 B47.94}69.204 8.661 24.269 { ca glu a 67 B47.75}66.314 6.731 22.717 { ca lys a 68 B45.81}66.596 6.323 18.949 { ca asp a 69 B42.85}63.531 6.899 16.792 { ca gly a 70 B34.95}64.600 7.885 13.282 { ca thr a 71 B38.80}61.214 8.970 11.949 { ca lys a 72 B41.13}61.708 11.831 9.486 { ca val a 73 B36.49}59.941 15.128 10.019 { ca asp a 74 B36.37}59.936 18.727 8.831 { ca ile a 75 B29.75}58.782 21.821 10.707 { ca thr a 76 B24.72}57.642 24.797 8.661 { ca tyr a 77 B23.02}57.796 28.266 10.220 { ca gly a 78 B22.50}56.855 31.581 8.653 { ca ser a 79 B28.29}60.589 32.238 8.363 { ca gly a 80 B23.92}61.400 28.875 6.817 { ca thr a 81 B24.00}61.534 25.083 7.160 { ca val a 82 B24.92}63.974 22.804 9.018 { ca lys a 83 B33.09}64.353 19.047 8.552 { ca gly a 84 B31.19}65.565 16.122 10.634 { ca phe a 85 B33.07}64.315 13.091 12.535 { ca phe a 86 B31.04}62.786 12.351 15.924 { ca ser a 87 B31.26}64.765 11.187 18.925 { ca lys a 88 B35.91}64.057 11.125 22.643 { ca asp a 89 B38.75}66.466 12.070 25.364 { ca leu a 90 B41.29}66.569 13.942 28.654 { ca val a 91 B42.53}65.531 17.571 28.321 { ca thr a 92 B36.98}66.547 20.072 30.989 { ca leu a 93 B37.07}65.006 23.497 31.546 { ca gly a 94 B40.22}66.199 25.386 34.601 { ca his a 95 B45.63}66.286 23.022 37.573 { ca leu a 96 B42.30}63.734 20.652 36.023 { ca ser a 97 B41.03}64.430 17.777 33.650 { ca met a 98 B44.44}62.550 14.995 31.830 { ca pro a 99 B44.88}62.737 12.489 28.918 { ca tyr a 100 B38.57}61.143 14.234 25.948 { ca lys a 101 B35.97}60.590 13.428 22.266 { ca phe a 102 B37.77}62.375 16.015 20.128 { ca ile a 103 B31.82}63.835 16.583 16.696 { ca glu a 104 B36.03}67.483 16.418 15.655 { ca val a 105 B32.85}67.669 18.873 12.787 { ca ile a 106 B34.38}70.035 17.916 9.986 { ca asp a 107 B34.71}69.002 20.536 7.449 { ca thr a 108 B33.96}68.691 24.280 8.013 { ca asp a 109 B33.80}69.319 25.844 4.590 { ca asp a 110 B33.34}65.724 27.020 4.185 { ca leu a 111 B31.68}65.980 28.917 7.478 { ca glu a 112 B31.24}68.736 31.139 6.064 { ca pro a 113 B34.36}69.796 33.883 6.025 { ca ile a 114 B35.77}68.074 34.285 9.429 { ca tyr a 115 B33.38}69.550 31.166 11.091 { ca ser a 116 B39.06}73.213 32.229 10.752 { ca ser a 117 B45.61}72.637 35.965 11.202 { ca val a 118 B48.80}71.113 35.553 14.687 { ca glu a 119 B55.28}72.264 33.476 17.633 { ca phe a 120 B42.77}70.169 30.498 18.697 { ca asp a 121 B39.06}70.798 26.830 18.037 { ca gly a 122 B33.65}67.288 25.448 18.235 { ca ile a 123 B27.28}63.697 26.183 19.135 { ca leu a 124 B27.37}61.514 25.005 21.975 { ca gly a 125 B24.89}57.817 25.135 21.208 { ca leu a 126 B23.42}55.390 26.156 23.934 { ca gly a 127 B28.29}52.150 25.856 21.958 { ca trp a 128 B27.98}49.533 23.108 22.270 { ca lys a 129 B34.81}49.539 19.466 21.251 { ca asp a 130 B34.28}47.620 19.917 17.983 { ca leu a 131 B30.70}50.109 22.576 16.873 { ca ser a 132 B28.09}52.915 20.014 17.021 { ca ile a 133 B30.88}53.938 17.526 14.391 { ca gly a 134 B37.13}53.980 14.071 15.960 { ca ser a 135 B45.04}51.285 14.623 18.605 { ca ile a 136 B33.68}53.618 15.673 21.393 { ca asp a 137 B38.56}52.224 16.827 24.731 { ca pro a 138 B31.22}53.512 20.250 25.782 { ca ile a 139 B32.80}56.394 19.817 28.187 { ca val a 140 B30.04}54.831 22.212 30.691 { ca val a 141 B36.90}51.771 19.965 30.629 { ca glu a 142 B46.18}54.129 16.994 31.105 { ca leu a 143 B44.67}55.885 18.607 34.059 { ca lys a 144 B49.84}52.623 19.483 35.769 { ca asn a 145 B52.22}51.382 15.915 35.378 { ca gln a 146 B53.66}54.644 14.597 36.834 { ca asn a 147 B48.56}54.128 17.112 39.660 { ca lys a 148 B39.76}57.375 19.010 39.192 { ca ile a 149 B38.19}55.575 22.394 39.101 { ca asp a 150 B41.72}52.557 23.878 40.912 { ca asn a 151 B38.82}50.579 24.862 37.807 { ca ala a 152 B37.90}50.522 23.954 34.130 { ca leu a 153 B32.76}51.364 27.519 33.124 { ca phe a 154 B27.52}54.301 29.708 32.100 { ca thr a 155 B25.80}54.932 33.424 31.832 { ca phe a 156 B28.09}57.007 35.704 29.650 { ca tyr a 157 B30.63}58.742 38.761 30.993 { ca leu a 158 B37.75}60.813 40.179 28.135 { ca pro a 159 B47.30}64.189 41.888 28.720 { ca val a 160 B63.22}65.007 45.534 28.086 { ca his a 161 B73.94}68.579 46.122 26.913 { ca asp a 162 B74.61}70.803 47.842 29.497 { ca val a 163 B66.24}67.919 47.981 31.946 { ca his a 164 B60.58}67.151 44.416 33.014 { ca ala a 165 B56.49}67.109 40.835 31.772 { ca gly a 166 B46.13}63.967 38.867 31.001 { ca tyr a 167 B39.55}62.645 35.586 32.318 { ca leu a 168 B28.18}60.584 32.627 31.192 { ca thr a 169 B30.88}58.897 31.415 34.364 { ca ile a 170 B31.82}57.382 27.940 34.470 { ca gly a 171 B28.54}55.004 26.795 37.200 { ca gly a 172 B31.21}53.620 29.931 38.827 { ca ile a 173 B36.16}52.945 33.660 38.503 { ca glu a 174 B47.24}55.607 35.999 39.970 { ca glu a 175 B46.82}54.089 39.370 40.960 { ca lys a 176 B45.28}57.375 41.290 40.666 { ca phe a 177 B38.40}57.118 41.227 36.853 { ca tyr a 178 B32.49}54.040 43.402 36.348 { ca glu a 179 B33.08}51.908 46.320 37.526 { ca gly a 180 B25.86}48.236 46.039 38.515 { ca asn a 181 B24.47}46.474 42.719 38.025 { ca ile a 182 B25.35}46.275 40.095 35.295 { ca thr a 183 B25.81}43.227 39.918 33.047 { ca tyr a 184 B24.02}42.629 36.741 31.063 { ca glu a 185 B24.83}41.283 36.046 27.593 { ca lys a 186 B31.39}39.926 32.574 26.760 { ca leu a 187 B28.86}41.492 30.796 23.770 { ca asn a 188 B24.44}39.293 30.296 20.703 { ca his a 189 B23.75}41.299 27.137 19.973 { ca asp a 190 B29.54}43.890 25.124 21.909 { ca leu a 191 B27.63}46.371 25.239 19.007 { ca tyr a 192 B20.17}48.398 28.453 19.159 { ca trp a 193 B19.14}47.775 30.784 22.070 { ca gln a 194 B21.53}45.044 32.450 20.044 { ca ile a 195 B22.35}42.150 34.629 21.234 { ca asp a 196 B21.66}39.329 36.794 19.864 { ca leu a 197 B22.36}39.953 40.544 19.838 { ca asp a 198 B29.43}38.594 43.506 17.928 { ca val a 199 B26.01}41.635 44.916 16.181 { ca his a 200 B27.31}41.883 48.697 15.885 { ca phe a 201 B32.72}44.758 50.124 13.796 { ca gly a 202 B38.80}43.583 53.722 13.881 { ca lys a 203 B47.33}40.296 53.884 11.991 { ca gln a 204 B42.19}40.883 50.452 10.485 { ca thr a 205 B39.70}38.963 47.797 12.374 { ca met a 206 B37.26}38.593 44.030 12.201 { ca glu a 207 B37.63}36.054 42.776 14.737 { ca lys a 208 B33.73}36.318 39.400 16.415 { ca ala a 209 B22.57}39.715 38.849 14.814 { ca asn a 210 B21.04}41.829 35.754 15.565 { ca val a 211 B19.42}44.940 36.885 17.433 { ca ile a 212 B19.10}48.013 34.777 18.097 { ca val a 213 B18.36}50.303 35.708 21.008 { ca asp a 214 B20.35}53.739 34.618 19.814 { ca ser a 215 B23.12}57.026 35.131 21.661 { ca gly a 216 B21.69}58.808 33.696 18.633 { ca thr a 217 B25.36}57.694 36.535 16.330 { ca thr a 218 B24.31}59.591 39.857 16.297 { ca thr a 219 B23.85}56.841 42.050 14.796 { ca ile a 220 B22.93}53.107 42.647 14.762 { ca thr a 221 B26.75}51.577 40.918 11.739 { ca ala a 222 B21.61}48.306 41.537 9.915 { ca pro a 223 B21.39}46.645 40.246 6.731 { ca ser a 224 B28.99}48.096 41.925 3.602 { ca glu a 225 B30.82}44.914 43.677 2.515 { ca phe a 226 B26.27}44.420 45.169 5.965 { ca leu a 227 B25.61}48.032 46.215 6.505 { ca asn a 228 B26.84}48.491 47.664 2.999 { ca lys a 229 B33.52}45.443 49.894 3.546 { ca phe a 230 B34.79}46.922 50.946 6.890 { ca phe a 231 B39.54}50.273 51.953 5.388 { ca ala a 232 B46.20}48.482 53.660 2.492 { ca asn a 233 B42.23}47.342 56.823 4.269 { ca leu a 234 B36.06}50.211 56.916 6.757 { ca asn a 235 B42.88}53.089 57.624 4.389 { ca val a 236 B44.03}54.759 54.308 5.119 { ca ile a 237 B37.04}57.219 53.212 2.447 { ca lys a 238 B30.95}58.165 49.620 1.738 { ca val a 239 B37.45}61.734 48.866 0.780 { ca pro a 240 B45.29}61.407 46.991 -2.528 { ca phe a 241 B49.93}61.372 43.180 -2.228 { ca leu a 242 B39.30}62.153 43.489 1.487 { ca pro a 243 B34.37}60.041 42.885 4.638 { ca phe a 244 B33.44}60.835 46.403 5.860 { ca tyr a 245 B29.75}58.600 49.426 6.168 { ca val a 246 B30.18}59.686 52.934 7.026 { ca thr a 247 B33.40}58.245 56.388 7.598 { ca thr a 248 B39.85}59.398 59.530 9.393 { ca cys a 249 B47.21}60.068 59.261 13.134 { ca asp a 250 B57.31}58.232 62.564 13.512 { ca asn a 251 B51.27}55.079 61.117 11.956 { ca lys a 252 B50.10}52.436 62.132 14.503 { ca glu a 253 B41.14}49.719 60.269 12.620 { ca met a 254 B35.50}50.875 56.769 13.608 { ca pro a 255 B31.36}47.991 55.662 15.891 { ca thr a 256 B28.82}47.951 53.734 19.140 { ca leu a 257 B26.43}46.911 50.174 18.345 { ca glu a 258 B29.44}43.867 48.890 20.228 { ca phe a 259 B24.80}42.890 45.288 20.928 { ca lys a 260 B29.88}39.570 44.942 22.704 { ca ser a 261 B28.46}37.780 41.917 24.093 { ca ala a 262 B38.98}34.364 42.090 25.748 { ca asn a 263 B42.98}35.815 43.163 29.115 { ca asn a 264 B30.19}39.342 44.380 28.397 { ca thr a 265 B25.90}41.430 46.660 26.243 { ca tyr a 266 B24.92}45.112 46.343 25.303 { ca thr a 267 B26.02}46.934 49.157 23.557 { ca leu a 268 B29.44}50.301 49.574 21.913 { ca glu a 269 B31.43}51.650 53.110 21.563 { ca pro a 270 B30.78}53.699 53.971 18.443 { ca glu a 271 B32.91}56.851 54.043 20.542 { ca tyr a 272 B22.35}56.536 50.267 20.823 { ca tyr a 273 B29.49}56.393 49.680 17.059 { ca met a 274 B39.31}58.709 52.367 15.640 { ca asn a 275 B44.73}62.505 52.545 15.702 { ca pro a 276 B45.96}64.972 55.046 14.231 { ca ile a 277 B47.31}66.964 53.302 11.503 { ca leu a 278 B55.27}70.323 54.994 12.083 { ca glu a 279 B64.50}71.848 55.453 15.540 { ca val a 280 B70.02}72.984 58.967 14.596 { ca asp a 281 B72.17}70.246 60.121 12.206 { ca asp a 282 B69.81}66.749 59.898 13.704 { ca thr a 283 B56.49}64.956 61.124 10.584 { ca leu a 284 B40.91}63.488 57.847 9.313 { ca cys a 285 B35.88}61.953 55.142 11.512 { ca met a 286 B32.25}61.286 51.458 10.931 { ca ile a 287 B29.33}57.740 50.189 11.485 { ca thr a 288 B32.92}57.696 46.895 13.370 { ca met a 289 B24.49}54.840 45.410 11.340 { ca leu a 290 B24.23}54.668 42.745 8.660 { ca pro a 291 B23.94}52.008 41.386 6.285 { ca val a 292 B28.90}51.349 37.699 6.856 { ca asp a 293 B33.10}48.406 35.932 5.295 { ca ile a 294 B31.82}47.481 32.898 7.356 { ca asp a 295 B36.09}43.771 33.509 6.705 { ca ser a 296 B33.38}41.431 36.490 6.334 { ca asn a 297 B28.16}41.417 37.636 9.971 { ca thr a 298 B23.07}44.467 36.277 11.792 { ca phe a 299 B22.59}46.933 38.622 13.471 { ca ile a 300 B24.09}50.175 37.874 15.300 { ca leu a 301 B18.75}51.134 39.897 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